| IED ID | IndEnz0002016254 |
| Enzyme Type ID | protease016254 |
| Protein Name |
Calpain small subunit 1 CSS1 Calcium-activated neutral proteinase small subunit CANP small subunit Calcium-dependent protease small subunit CDPS Calcium-dependent protease small subunit 1 Calpain regulatory subunit |
| Gene Name | CAPNS1 CAPN4 |
| Organism | Sus scrofa (Pig) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | MFLVNSFLKGGGGGGGGGGGLGGGLGNVLGGLISGAGGGGGGGGGGGGGGGGGGTAMRILGGVISAISEAAAQYNPEPPPPRTHYSNIEANESEEVRQFRRLFAQLAGDDMEVSATELMNILNKVVTRHPDLKTDGFGIDTCRSMVAVMDSDTTGKLGFEEFKYLWNNIKKWQAIYKQFDVDRSGTIGSSELPGAFEAAGFHLNEHLYSMIIRRYSDEGGNMDFDNFISCLVRLDAMFRAFKSLDKDGTGQIQVNIQEWLQLTMYS |
| Enzyme Length | 266 |
| Uniprot Accession Number | P04574 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | CA_BIND 106..117; /note=1; /evidence=ECO:0000250|UniProtKB:Q64537; CA_BIND 150..161; /note=2; /evidence=ECO:0000250|UniProtKB:Q64537; CA_BIND 180..191; /note=3; /evidence=ECO:0000250|UniProtKB:Q64537 |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Essential for embryonic development (By similarity). {ECO:0000250|UniProtKB:O88456}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (5); Calcium binding (3); Chain (1); Domain (5); Helix (8); Metal binding (16); Modified residue (3); Turn (2) |
| Keywords | 3D-structure;Acetylation;Calcium;Cell membrane;Cytoplasm;Membrane;Metal-binding;Phosphoprotein;Reference proteome;Repeat |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Translocates to the plasma membrane upon calcium binding. {ECO:0000250}. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000250|UniProtKB:P04632; MOD_RES 6; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P04632; MOD_RES 177; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P04632 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (7) |
| Cross Reference PDB | 1ALV; 1ALW; 1NX0; 1NX1; 1NX2; 1NX3; 4PHN; |
| Mapped Pubmed ID | 25086406; |
| Motif | |
| Gene Encoded By | |
| Mass | 28,068 |
| Kinetics | |
| Metal Binding | METAL 107; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 110; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 112; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 117; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 135; /note=Calcium 4; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 150; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 152; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 154; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 156; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 161; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 180; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 182; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 184; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 186; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 191; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 223; /note=Calcium 4; /evidence=ECO:0000250|UniProtKB:Q64537 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.B24; |